Crystallization and preliminary X-ray analysis of methylthioribose-1-phosphate isomerase from Bacillus subtilis

被引：1

作者：

Tamura, H

Matsumura, H

Inoue, T

Ashida, H

Saito, Y

Yokota, A

Kai, Y

机构：

[1] Osaka Univ, Grad Sch Engn, Dept Chem Mat, Suita, Osaka 5650871, Japan

[2] Japan Sci & Technol Agcy, PRESTO, Struct & Funct Biomol Grp, Kawaguchi, Saitama, Japan

[3] Nara Inst Sci & Technol, Grad Sch Biol Sci, Dept Biol Mol, Ikoma, Nara 6300101, Japan

来源：

ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2005年 / 61卷

关键词：

D O I：

10.1107/S1744309105015757

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

Methylthioribose-1-phosphate isomerase (MtnA) from Bacillus subtilis, the first enzyme in the downstream section of the methionine-salvage pathway, was crystallized using the sitting-drop vapour-diffusion method. Crystals grew using ammonium sulfate as the precipitant at 293 K. They diffracted to 2.5 angstrom at 100 K using synchrotron radiation and were found to belong to the tetragonal space group P4(1), with unit-cell parameters a = b = 69.2, c = 154.7 angstrom. The asymmetric unit contains two molecules of MtnA, with a V-M value of 2.4 angstrom(3) Da(-1) and a solvent content of 48%.

引用

页码：595 / 598

页数：4

共 20 条

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